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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yilmaz, Duygu Koçer, Armagan Li, Zhuolun Konijnenberg, Albert Sobott, Frank Dimitrova, Anna Ingólfsson, Helgi I. Marrink, Siewert J. Vénien-bryan, Catherine |
| Description | Author Affiliation: Konijnenberg A ( Biomolecular & Analytical Mass Spectrometry Group and.); Yilmaz D ( Department of Biochemistry and.); Ingólfsson HI ( Department of Biochemistry and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG, Groningen, The Netherlands); Dimitrova A ( Department of Biochemistry and.); Marrink SJ ( Department of Biochemistry and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG, Groningen, The Netherlands); Li Z ( Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie, Sorbonne Universités, CNRS UMR 7590, Université Pierre et Marie Curie, 75005 Paris, France); Vénien-Bryan C ( Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie, Sorbonne Universités, CNRS UMR 7590, Université Pierre et Marie Curie, 75005 Paris, France); Sobott F ( Biomolecular & Analytical Mass Spectrometry Group and UA-VITO Center for Proteomics (CFP-CEPROMA), University of Antwerp, 2020 Antwerp, Belgium); Koçer A ( Department of Neuroscience, University of Groningen, University Medical Center Groningen, 9713 AV, Groningen, The Netherlands a.kocer@umcg.nl frank.sobott@uantwerpen.be.); |
| Abstract | Mechanosensitive ion channels are sensors probing membrane tension in all species; despite their importance and vital role in many cell functions, their gating mechanism remains to be elucidated. Here, we determined the conditions for releasing intact mechanosensitive channel of large conductance (MscL) proteins from their detergents in the gas phase using native ion mobility-mass spectrometry (IM-MS). By using IM-MS, we could detect the native mass of MscL from Escherichia coli, determine various global structural changes during its gating by measuring the rotationally averaged collision cross-sections, and show that it can function in the absence of a lipid bilayer. We could detect global conformational changes during MscL gating as small as 3%. Our findings will allow studying native structure of many other membrane proteins. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 48 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Ion Channel Gating Physiology Ion Channels Metabolism Mass Spectrometry Mechanotransduction, Cellular Detergents Chemistry Escherichia Coli Escherichia Coli Proteins Ultrastructure Membrane Proteins Microscopy, Electron Molecular Dynamics Simulation Octoxynol Protein Conformation Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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